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dc.contributor.authorLiebau, Jessica
dc.contributor.authorLaatsch, Bethany
dc.contributor.authorLowater, Harrison
dc.contributor.authorHati, Sanchita
dc.descriptionColor poster with text, charts, images, and graphs.en_US
dc.description.abstractPoly(ethylene glycol) (PEG) is a biocompatible, hydrophilic, flexible, non-toxic polyether commonly used in proteomics because it is widely regarded to be a biologically inert molecule. This includes PEG2000 (molecular weight of 2000g/mol), which is a component in the Pfizer-BioNTech and Moderna COVID-19 vaccines. However, recent studies suggest that PEG may impact protein function, depending largely on the molecular weight of the PEG. In this study, we observe the effects of PEG on the function and conformation of enzyme prolyl-tRNA synthetase of Escherichia coli (Ec ProRS). ProRS catalyzes the covalent attachment of proline to tRNAPro and thus is essential for protein biosynthesis. The molecular mechanism of PEG-protein interactions has been probed using enzyme kinetics, fluorescence spectroscopy, and molecular modeling. Herein, we present the results of our study.en_US
dc.description.sponsorshipNational Institute of Health (Grant#:1R15GM117510); University of Wisconsin--Eau Claire Office of Research and Sponsored Programsen_US
dc.relation.ispartofseriesUSGZE AS589;
dc.subjectPolyethylene glycolen_US
dc.subjectEscherichia colien_US
dc.subjectFluorescence spectroscopyen_US
dc.subjectDepartment of Chemistry and Biochemistryen_US
dc.titleHow Does Varying Sizes and Concentrations of Poly(Ethylene Glycol) Affect the Conformation and Function of the Enzyme Escherichia Coli Prolyl-Trna Synthetase?en_US

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